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Merck
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MABF2158

Sigma-Aldrich

Anti-TMPRSS2 Antibody, clone P5H9-A3

clone P5H9-A3, from mouse

Szinonimák:

Transmembrane protease serine 2, Serine protease 10

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352203
eCl@ss:
32160702
NACRES:
NA.43

biológiai forrás

mouse

antitest forma

purified antibody

antitest terméktípus

primary antibodies

klón

P5H9-A3, monoclonal

faj reaktivitás

human

kiszerelés

antibody small pack of 25 μg

technika/technikák

ELISA: suitable
immunohistochemistry: suitable (paraffin)
western blot: suitable

izotípus

IgG1κ

UniProt elérési szám

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... TMPRSS2(7113)

Related Categories

Általános leírás

Transmembrane protease serine 2 (UniProt: O15393; also known as Serine protease 10, TMPRSS2) is encoded by the TMPRSS2 (also known as PRSS10) gene (Gene ID: 7113) in human. TMPRSS2 is a single-pass type II membrane protein of the peptidase S1 family that is shown to proteolytically cleave and activate the viral spike glycoproteins, which facilitate virus-cell membrane fusions. It is shown to facilitate human SARS coronavirus (SARS-CoV) infection via two independent mechanisms, proteolytic cleavage of ACE2 that promotes viral uptake and cleavage of coronavirus spike glycoprotein, which activates the glycoprotein for cathepsin L-independent host cell entry. TMPRSS2 is highly expressed in the prostate tissue and lower expression levels are observed in the epithelia of the colon, stomach, epididymis and breast tissue. Some expression has also been reported in pancreatic acini, hepatic bile ducts, testicular Leydig cells and the kidney. Its expression levels are significantly elevated in both neoplastic prostate and in the epithelium of prostatic hyperplasia. TMPRSS2 has a cytoplasmic domain (aa 1-84), a transmembrane domain (aa 85-105), and an extracellular domain (aa 106-492). Its peptidase S1 domain is localized to amino acids 256-489. It is reported to be proteolytically processed by an autocatalytic mechanism generating the transmembrane protease serine 2 non-catalytic chain (1-255) and the transmembrane protease serine 2 catalytic chain (256-492). Two isoforms of TMPRSS2 have been described that are produced by alternative splicing.

Egyediség

Clone P5H9-A3 specifically detects human Transmembrane protease serine 2. It targets an epitope with in the extracellular serine protease domain.

Immunogen

KLH-conjugated linear peptide corresponding to 16 amino acids from the extracellular domain of human transmembrane protease serine 2.

Alkalmazás

Anti-TMPRSS2, clone P5H9-A3, Cat. No. MABF2158, is a mouse monoclonal antibody that detects Transmembrane protease serine 2 and has been tested for use in ELISA, Immunohistochemistry (Paraffin), and Western Blotting.
Immunohistochemistry (Paraffin) Analysis: 1:50 dilution from a representative lot detected TMPRSS2 in human kidney tissue sections.

Enzyme Immunoassay (ELISA) Analysis: A representative lot detected TMPRSS2 in ELISA applications (Lucas, J.M., et. al. (2008). J Pathol. 215(2):118-25).

Western Blotting Analysis: A representative lot detected TMPRSS2 in Western Blotting applications (Lucas, J.M., et. al. (2008). J Pathol. 215(2):118-25).

Immunohistochemistry (Paraffin) Analysis: A representative lot detected TMPRSS2 in Immunohistochemistry applications (Lucas, J.M., et. al. (2008). J Pathol. 215(2):118-25; Bertram, S., et. al. (2012). PLoS One. 7(4):e35876).
Research Category
Inflammation & Immunology

Minőség

Evaluated by Immunohistochemistry (Paraffin) in human prostate tissue sections.

Immunohistochemistry (Paraffin) Analysis: 1:250 dilution of this antibody detected TMPRSS2 in human prostate tissue sections.

Cél megnevezése

53.86 kDa calculated.

Fizikai forma

Format: Purified
Protein G purified
Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Tárolás és stabilitás

Stable for 1 year at 2-8°C from date of receipt.

Egyéb megjegyzések

Concentration: Please refer to lot specific datasheet.

Jogi nyilatkozat

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Dokumentumtár megtekintése

Jessica M Vanslambrouck et al.
Nature communications, 13(1), 5943-5943 (2022-10-09)
While pluripotent stem cell-derived kidney organoids are now being used to model renal disease, the proximal nephron remains immature with limited evidence for key functional solute channels. This may reflect early mispatterning of the nephrogenic mesenchyme and/or insufficient maturation. Here
Chaitanya Gandikota et al.
Journal of medical virology, 96(4), e29579-e29579 (2024-04-04)
Severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) primarily targets the respiratory system. Physiologically relevant human lung models are indispensable to investigate virus-induced host response and disease pathogenesis. In this study, we generated human induced pluripotent stem cell (iPSC)-derived alveolar organoids (AOs)
Florian Sure et al.
The Journal of biological chemistry, 298(6), 102004-102004 (2022-05-04)
The epithelial sodium channel (ENaC) is a heterotrimer consisting of α-, β-, and γ-subunits. Channel activation requires proteolytic release of inhibitory tracts from the extracellular domains of α-ENaC and γ-ENaC; however, the proteases involved in the removal of the γ-inhibitory
Laurensius Kevin Lie et al.
Virology, 588, 109889-109889 (2023-10-02)
The lack of suitable in vitro culture model has hampered research on wild-type (WT) human coronaviruses. While 3D tissue or organ cultures have been instrumental for this purpose, such models are challenging, time-consuming, expensive and require extensive cell culture adaptation
Tsuguhisa Nakayama et al.
Cell reports. Medicine, 2(10), 100421-100421 (2021-10-05)
Understanding viral tropism is an essential step toward reducing severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) transmission, decreasing mortality from coronavirus disease 2019 (COVID-19) and limiting opportunities for mutant strains to arise. Currently, little is known about the extent to

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